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Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties
REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be involved in defense/stress mechanisms after ta...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3485013/ https://www.ncbi.nlm.nih.gov/pubmed/23133547 http://dx.doi.org/10.1371/journal.pone.0048065 |
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author | Berthelot, Karine Lecomte, Sophie Estevez, Yannick Coulary-Salin, Bénédicte Bentaleb, Ahmed Cullin, Christophe Deffieux, Alain Peruch, Frédéric |
author_facet | Berthelot, Karine Lecomte, Sophie Estevez, Yannick Coulary-Salin, Bénédicte Bentaleb, Ahmed Cullin, Christophe Deffieux, Alain Peruch, Frédéric |
author_sort | Berthelot, Karine |
collection | PubMed |
description | REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be involved in defense/stress mechanisms after tapping or directly acting on the isoprenoid biosynthetic pathway. The structure of these two proteins is still not described. In this work, it was discovered that REF has amyloid properties, contrary to SRPP. We investigated their structure by CD, TEM, ATR-FTIR and WAXS and neatly showed the presence of β-sheet organized aggregates for REF, whereas SRPP mainly fold as a helical protein. Both proteins are highly hydrophobic but differ in their interaction with lipid monolayers used to mimic the monomembrane surrounding the rubber particles. Ellipsometry experiments showed that REF seems to penetrate deeply into the monolayer and SRPP only binds to the lipid surface. These results could therefore clarify the role of these two paralogous proteins in latex production, either in the coagulation of natural rubber or in stress-related responses. To our knowledge, this is the first report of an amyloid formed from a plant protein. This suggests also the presence of functional amyloid in the plant kingdom. |
format | Online Article Text |
id | pubmed-3485013 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34850132012-11-06 Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties Berthelot, Karine Lecomte, Sophie Estevez, Yannick Coulary-Salin, Bénédicte Bentaleb, Ahmed Cullin, Christophe Deffieux, Alain Peruch, Frédéric PLoS One Research Article REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be involved in defense/stress mechanisms after tapping or directly acting on the isoprenoid biosynthetic pathway. The structure of these two proteins is still not described. In this work, it was discovered that REF has amyloid properties, contrary to SRPP. We investigated their structure by CD, TEM, ATR-FTIR and WAXS and neatly showed the presence of β-sheet organized aggregates for REF, whereas SRPP mainly fold as a helical protein. Both proteins are highly hydrophobic but differ in their interaction with lipid monolayers used to mimic the monomembrane surrounding the rubber particles. Ellipsometry experiments showed that REF seems to penetrate deeply into the monolayer and SRPP only binds to the lipid surface. These results could therefore clarify the role of these two paralogous proteins in latex production, either in the coagulation of natural rubber or in stress-related responses. To our knowledge, this is the first report of an amyloid formed from a plant protein. This suggests also the presence of functional amyloid in the plant kingdom. Public Library of Science 2012-10-25 /pmc/articles/PMC3485013/ /pubmed/23133547 http://dx.doi.org/10.1371/journal.pone.0048065 Text en © 2012 Berthelot et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Berthelot, Karine Lecomte, Sophie Estevez, Yannick Coulary-Salin, Bénédicte Bentaleb, Ahmed Cullin, Christophe Deffieux, Alain Peruch, Frédéric Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title | Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title_full | Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title_fullStr | Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title_full_unstemmed | Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title_short | Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties |
title_sort | rubber elongation factor (ref), a major allergen component in hevea brasiliensis latex has amyloid properties |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3485013/ https://www.ncbi.nlm.nih.gov/pubmed/23133547 http://dx.doi.org/10.1371/journal.pone.0048065 |
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